pubmed-article:1715320 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1715320 | lifeskim:mentions | umls-concept:C0038409 | lld:lifeskim |
pubmed-article:1715320 | lifeskim:mentions | umls-concept:C0003241 | lld:lifeskim |
pubmed-article:1715320 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:1715320 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:1715320 | lifeskim:mentions | umls-concept:C0055948 | lld:lifeskim |
pubmed-article:1715320 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:1715320 | lifeskim:mentions | umls-concept:C0061365 | lld:lifeskim |
pubmed-article:1715320 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
pubmed-article:1715320 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:1715320 | pubmed:dateCreated | 1991-10-2 | lld:pubmed |
pubmed-article:1715320 | pubmed:abstractText | A 10-amino-acid repeating sequence of the hemagglutinating portion of Clostridium difficile toxin A has been synthesized and used to produce antisera in rabbits. Antipeptide antibody inhibited toxin A-mediated hemagglutination and neutralized cytotoxic activity. Immunoblot analysis with the antipeptide antibody revealed cross-reactivity with native toxin, a recombinant protein containing the toxin A repeats, and a glucan-binding protein from Streptococcus mutans whose primary structure has repeating amino acid motifs similar to those of the synthetic peptide. A polyclonal antibody against the glucan-binding protein, which cross-reacted with purified toxin A, also inhibited toxin A-mediated hemagglutination and neutralized cytotoxic activity. We recently identified toxin A and the glucan-binding protein as members of a novel family of clostridial and streptococcal binding proteins based on conserved repeating amino acid motifs at the C-terminal region of the molecules. This study provides immunological and functional evidence of the predicted relationship between toxin A and the glucan-binding protein and further implicates the repeating subunits as ligand-binding domains in this family of proteins. | lld:pubmed |
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pubmed-article:1715320 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1715320 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1715320 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1715320 | pubmed:month | Sep | lld:pubmed |
pubmed-article:1715320 | pubmed:issn | 0019-9567 | lld:pubmed |
pubmed-article:1715320 | pubmed:author | pubmed-author:TabaqchaliSS | lld:pubmed |
pubmed-article:1715320 | pubmed:author | pubmed-author:RussellR RRR | lld:pubmed |
pubmed-article:1715320 | pubmed:author | pubmed-author:WrenB WBW | lld:pubmed |
pubmed-article:1715320 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1715320 | pubmed:volume | 59 | lld:pubmed |
pubmed-article:1715320 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1715320 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1715320 | pubmed:pagination | 3151-5 | lld:pubmed |
pubmed-article:1715320 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:1715320 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1715320 | pubmed:articleTitle | Antigenic cross-reactivity and functional inhibition by antibodies to Clostridium difficile toxin A, Streptococcus mutans glucan-binding protein, and a synthetic peptide. | lld:pubmed |
pubmed-article:1715320 | pubmed:affiliation | Department of Medical Microbiology, St. Bartholomew's Hospital Medical College, West Smithfield, London, United Kingdom. | lld:pubmed |
pubmed-article:1715320 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1715320 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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